Literature summary for 3.5.3.1 extracted from

Wells, G.A.; Mueller, I.B.; Wrenger, C.; Louw, A.I.
The activity of Plasmodium falciparum arginase is mediated by a novel inter-monomer salt-bridge between Glu295-Arg404 (2009), FEBS J., 276, 3517-3530.

Crystallization (Commentary)

Crystallization (Comment)	Organism
homology modelling and molecular dynamics study on the mechanism of metal dependency. When the active site metals are removed, loss of structural integrity is observed reflected by a larger equilibration root mean square deviation for the protein when the active site metal is removed and some loss of secondary structure. An inter-monomer salt-bridge between Glu295 and Arg404 is associated with the metal dependency	Plasmodium falciparum 3D7

Crystallization (Comment)

Organism

homology modelling and molecular dynamics study on the mechanism of metal dependency. When the active site metals are removed, loss of structural integrity is observed reflected by a larger equilibration root mean square deviation for the protein when the active site metal is removed and some loss of secondary structure. An inter-monomer salt-bridge between Glu295 and Arg404 is associated with the metal dependency

Plasmodium falciparum 3D7

Protein Variants

Protein Variants	Comment	Organism
E295A	96% decrease in activity. Residue is not involved in inter-monomer salt bridge	Plasmodium falciparum 3D7
E295A/R404A	95% decrease in activity	Plasmodium falciparum 3D7
E295R	73% decrease in activity	Plasmodium falciparum 3D7
R404A	54% decrease in activity, lack of trimer association. Residue is not involved in inter-monomer salt bridge	Plasmodium falciparum 3D7

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
13	-	L-arginine	wild-type, pH 8.0, temperature not specified in the publication	Plasmodium falciparum 3D7
45	-	L-arginine	mutant R404A, pH 8.0, temperature not specified in the publication	Plasmodium falciparum 3D7
146	-	L-arginine	mutant E295R, pH 8.0, temperature not specified in the publication	Plasmodium falciparum 3D7

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Magnesium	stabilizes the protein. In the absence of Mg2+, a complete loss of secondary structure is observed for certain elements	Plasmodium falciparum 3D7
Manganese	the more deeply buried Mn2+ ion A is coordinated by residues His193, Asp216, Asp220 and Asp323. The second metal, Mn2+B is co-ordinated by His218, Asp216, Asp323, Asp325	Plasmodium falciparum 3D7

Organism

Organism	UniProt	Comment	Textmining
Plasmodium falciparum 3D7	Q8I384	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-arginine + H2O	-	Plasmodium falciparum 3D7	L-ornithine + urea	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
1	-	L-arginine	mutant E295A, pH 8.0, temperature not specified in the publication	Plasmodium falciparum 3D7
1.3	-	L-arginine	mutant E295A/R404A, pH 8.0, temperature not specified in the publication	Plasmodium falciparum 3D7
6.7	-	L-arginine	mutant E295R, pH 8.0, temperature not specified in the publication	Plasmodium falciparum 3D7
11.4	-	L-arginine	mutant R404A, pH 8.0, temperature not specified in the publication	Plasmodium falciparum 3D7
24.8	-	L-arginine	wild-type, pH 8.0, temperature not specified in the publication	Plasmodium falciparum 3D7

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism
0.03	-	L-arginine	mutant E295R, pH 8.0, temperature not specified in the publication	Plasmodium falciparum 3D7
0.25	-	L-arginine	mutant R404A, pH 8.0, temperature not specified in the publication	Plasmodium falciparum 3D7
1.9	-	L-arginine	wild-type, pH 8.0, temperature not specified in the publication	Plasmodium falciparum 3D7